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Journal Article

Identification of Synaptophysin as a Hexameric Channel Protein of the Synaptic Vesicle Membrane

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Hartung,  Klaus
Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society;

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Bamberg,  Ernst
Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Thomas, L., Hartung, K., Langosch, D., Rehm, H., Bamberg, E., Franke, W. W., et al. (1988). Identification of Synaptophysin as a Hexameric Channel Protein of the Synaptic Vesicle Membrane. Science, 242(4881), 1050-1053. doi:10.1126/science.2461586.


Cite as: http://hdl.handle.net/21.11116/0000-0007-9930-6
Abstract
The quaternary structure and functional properties of synaptophysin, a major integral membrane protein of small presynaptic vesicles, were investigated. Cross-linking and sedimentation studies indicate that synaptophysin is a hexameric homo-oligomer, which in electron micrographs exhibits structural features common to channel-forming proteins. On reconstitution into planar lipid bilayers, purified synaptophysin displays voltage-sensitive channel activity with an average conductance of about 150 picosiemens. Because specific channels and fusion pores have been implicated in vesicular uptake and release of secretory compounds, synaptophysin may have a role in these processes.